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Osmotic pressure induced tensile forces in tendon collagen

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      Abstract

      Water is an important component of collagen in tendons, but its role for the function of this load-carrying protein structure is poorly understood. Here we use a combination of multi-scale experimentation and computation to show that water is an integral part of the collagen molecule, which changes conformation upon water removal. The consequence is a shortening of the molecule that translates into tensile stresses in the range of several to almost 100 MPa, largely surpassing those of about 0.3 MPa generated by contractile muscles. Although a complete drying of collagen would be relevant for technical applications, such as the fabrication of leather or parchment, stresses comparable to muscle contraction already occur at small osmotic pressures common in biological environments. We suggest, therefore, that water-generated tensile stresses may play a role in living collagen-based materials such as tendon or bone.

      Abstract

      Water is an important component of collagen in tendons, bone and extracellular matrix, but its role in the mechanical function of protein is poorly understood. Here, the authors study the effects of osmotic pressure on contraction in collagen, suggesting that collagen could function as a mechanical actuator.

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      Most cited references 36

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      The variation in isometric tension with sarcomere length in vertebrate muscle fibres.

      1. The variation of isometric tetanus tension with sarcomere length in single fibres from frog striated muscle has been re-investigated with special precautions to ensure uniformity of sarcomere length within the part of the fibre being studied.2. In most respects the results of Ramsey & Street (1940) were confirmed, but (a) the peak of the curve was found to consist of a plateau between sarcomere lengths of 2.05 and 2.2 mu, (b) the decline of tension above this plateau is steeper than found by Ramsey & Street, and (c) the decline of tension below the plateau becomes suddenly steeper at a sarcomere length of about 1.67 mu.3. Many features of this length-tension relation are simply explained on the sliding-filament theory.4. It is concluded that, in the plateau and at greater lengths, the tension on each thin filament is made up of equal contributions from each bridge which it overlaps on adjacent thick filaments.5. Internal resistance to shortening is negligible in this range but becomes progressively more important with shortening below the plateau.
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        Microfibrillar structure of type I collagen in situ.

        The fibrous collagens are ubiquitous in animals and form the structural basis of all mammalian connective tissues, including those of the heart, vasculature, skin, cornea, bones, and tendons. However, in comparison with what is known of their production, turnover and physiological structure, very little is understood regarding the three-dimensional arrangement of collagen molecules in naturally occurring fibrils. This knowledge may provide insight into key biological processes such as fibrillo-genesis and tissue remodeling and into diseases such as heart disease and cancer. Here we present a crystallographic determination of the collagen type I supermolecular structure, where the molecular conformation of each collagen segment found within the naturally occurring crystallographic unit cell has been defined (P1, a approximately 40.0 A, b approximately 27.0 A, c approximately 678 A, alpha approximately 89.2 degrees , beta approximately 94.6 degrees , gamma approximately 105.6 degrees ; reflections: 414, overlapping, 232, and nonoverlapping, 182; resolution, 5.16 A axial and 11.1 A equatorial). This structure shows that the molecular packing topology of the collagen molecule is such that packing neighbors are arranged to form a supertwisted (discontinuous) right-handed microfibril that interdigitates with neighboring microfibrils. This interdigitation establishes the crystallographic superlattice, which is formed of quasihexagonally packed collagen molecules. In addition, the molecular packing structure of collagen shown here provides information concerning the potential modes of action of two prominent molecules involved in human health and disease: decorin and the Matrix Metallo-Proteinase (MMP) collagenase.
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          Nature designs tough collagen: explaining the nanostructure of collagen fibrils.

          Collagen is a protein material with superior mechanical properties. It consists of collagen fibrils composed of a staggered array of ultra-long tropocollagen (TC) molecules. Theoretical and molecular modeling suggests that this natural design of collagen fibrils maximizes the strength and provides large energy dissipation during deformation, thus creating a tough and robust material. We find that the mechanics of collagen fibrils can be understood quantitatively in terms of two critical molecular length scales chi(S) and chi(R) that characterize when (i) deformation changes from homogeneous intermolecular shear to propagation of slip pulses and when (ii) covalent bonds within TC molecules begin to fracture, leading to brittle-like failure. The ratio chi(S)/chi(R) indicates which mechanism dominates deformation. Our modeling rigorously links the chemical properties of individual TC molecules to the macroscopic mechanical response of fibrils. The results help to explain why collagen fibers found in nature consist of TC molecules with lengths in the proximity of 300 nm and advance the understanding how collagen diseases that change intermolecular adhesion properties influence mechanical properties.
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            Author and article information

            Affiliations
            [1 ]Department of Biomaterials, Max Planck Institute for Colloids and Interfaces , Research Campus Golm, 14424 Potsdam, Germany
            [2 ]Laboratory for Atomistic and Molecular Mechanics, Department of Civil and Environmental Engineering, MIT , Cambridge, Massachusetts 02139, USA
            Author notes
            [*]

            These authors contributed equally to this work

            Journal
            Nat Commun
            Nat Commun
            Nature Communications
            Nature Pub. Group
            2041-1723
            22 January 2015
            : 6
            25608644
            4354200
            ncomms6942
            10.1038/ncomms6942
            Copyright © 2015, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.

            This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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